ID A0A150HCB8_9MICO Unreviewed; 566 AA.
AC A0A150HCB8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Ribonuclease J {ECO:0000256|HAMAP-Rule:MF_01491};
DE Short=RNase J {ECO:0000256|HAMAP-Rule:MF_01491};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01491};
GN Name=rnj {ECO:0000256|HAMAP-Rule:MF_01491};
GN ORFNames=Bravens_00224 {ECO:0000313|EMBL:KXZ59752.1};
OS Brevibacterium ravenspurgense.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=479117 {ECO:0000313|EMBL:KXZ59752.1, ECO:0000313|Proteomes:UP000243589};
RN [1] {ECO:0000313|EMBL:KXZ59752.1, ECO:0000313|Proteomes:UP000243589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG56047 {ECO:0000313|EMBL:KXZ59752.1,
RC ECO:0000313|Proteomes:UP000243589};
RA Bernier A.-M., Burdz T., Huynh C., Pachecho A.L., Wiebe D., Bonner C.,
RA Bernard K.;
RT "Use of Whole Genome Sequencing to ascertain that Brevibacterium
RT massiliense (Roux, Raoult 2009) is a later heterotypic synonym of
RT Brevibacterium ravenspurgense (Mages 2008).";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: An RNase that has 5'-3' exonuclease and possibly endonuclease
CC activity. Involved in maturation of rRNA and in some organisms also
CC mRNA maturation and/or decay. {ECO:0000256|HAMAP-Rule:MF_01491}.
CC -!- SUBUNIT: Homodimer, may be a subunit of the RNA degradosome.
CC {ECO:0000256|HAMAP-Rule:MF_01491}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01491}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. Bacterial RNase J
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01491}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXZ59752.1}.
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DR EMBL; LQQC01000002; KXZ59752.1; -; Genomic_DNA.
DR RefSeq; WP_062019545.1; NZ_LQQC01000002.1.
DR AlphaFoldDB; A0A150HCB8; -.
DR PATRIC; fig|479117.4.peg.221; -.
DR Proteomes; UP000243589; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004534; F:5'-3' RNA exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR CDD; cd07714; RNaseJ_MBL-fold; 1.
DR Gene3D; 3.10.20.580; -; 1.
DR Gene3D; 3.40.50.10710; Metallo-hydrolase/oxidoreductase; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR HAMAP; MF_01491; RNase_J_bact; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR InterPro; IPR004613; RNase_J.
DR InterPro; IPR042173; RNase_J_2.
DR InterPro; IPR030854; RNase_J_bac.
DR InterPro; IPR041636; RNase_J_C.
DR NCBIfam; TIGR00649; MG423; 1.
DR PANTHER; PTHR43694; RIBONUCLEASE J; 1.
DR PANTHER; PTHR43694:SF1; RIBONUCLEASE J; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF07521; RMMBL; 1.
DR Pfam; PF17770; RNase_J_C; 1.
DR PIRSF; PIRSF004803; RnjA; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01491};
KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_01491};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01491};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01491};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01491};
KW Reference proteome {ECO:0000313|Proteomes:UP000243589};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01491}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_01491};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 31..218
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 374..378
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 566 AA; 61619 MW; 6625E9C8C4F456DB CRC64;
MIELPTDLGT PPKVDPNALR IVALGGLGEV GRNMTVFETD GKLLIIDAGV LFPEEEQPGV
DLILPDFSYL DGREKDVVGI ALTHGHEDHI GAVPYLLRKL GRDVPILGST LTLALVEPKL
KEHRVRAKTK VVSEGDREKL GPFDLEFIAV NHSIPDALAI FLRTDAGTIL HTGDFKMDQL
PLDGRITDLR SFARVGEEGV DLFLTDSTNA EVPGFTAHER NIGRVLEQQF SHASRRVIVA
SFASHVHRVQ QVLEAAVAHG RKVAFVGRSM VRNMKIAQEL GYLQAPAGSI IDIKQVEDLP
EDQVVLMCTG SQGEPMAALS RMANGTHQID LTEGDTVILA SSLIPGNENS VSRVINGLMR
LGATVIHKGN AAVHVSGHAS AGELLYAYNI VGPKGVMPVH GEWRHMLANA KLAMETGVPK
EKVVVADDGW VVDLKDGQAS IVGAVPCEYV FVDGKSVGYV TEDDLRDRRV LAGEGFVSIF
MTIDVKNREI VAGPEIHTRG VAEHDRVFDT IKPKITKAVE EALDDGVKNQ HRLQQIIRRT
IGRWLSTKLR RGPMIVPMVV LVGDED
//
